Structure of PDB 5ybh Chain A

Receptor sequence
>5ybhA (length=334) Species: 623 (Shigella flexneri) [Search protein sequence]
GSHMHTQVGRGLLGAVVNPLGEVTDKFAVTDNSEILYRPVDNAPPLYSER
AAIEKPFLTGIKVIDSLLTCGEGQRMGIFASAGCGKTFLMNMLIEHSGAD
IYVIGLIGERGREVTETVDYLKNSEKKSRCVLVYATSDYSSVDRCNAAYI
ATAIAEFFRTEGHKVALFIDSLTRYARALRDVALAAGESPARRGYPVSVF
DSLPRLLERPGKLKAGGSITAFYTVLLEDDDFADPLAEEVRSILDGHIYL
SRNLAQKGQFPAIDSLKSISRVFTQVVDEKHRIMAAAFRELLSEIEELRT
IYNKISVVESFLKQDYRLGFTYEQTMELIGETIR
3D structure
PDB5ybh Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromShigella flexneri
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K165 E188 R189 R350
Catalytic site (residue number reindexed from 1) K86 E109 R110 R271
Enzyme Commision number 7.4.2.8: protein-secreting ATPase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A G139 D144 F416 T417 T421 G60 D65 F320 T321 T325
BS02 MG A R117 N121 R38 N42
BS03 MG A T252 D313 T173 D234
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0009058 biosynthetic process
GO:0030254 protein secretion by the type III secretion system
Cellular Component
GO:0005737 cytoplasm
GO:0030257 type III protein secretion system complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ybh, PDBe:5ybh, PDBj:5ybh
PDBsum5ybh
PubMed30013545
UniProtP0A1C1|SCTN_SHIFL Type 3 secretion system ATPase (Gene Name=sctN)

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